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Sequence of IPNA_ACRCH

EC Number:1.21.3.1

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
isopenicillin-N synthase
P05189
Acremonium chrysogenum
338
38433
Reaction
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O
Other sequences found for EC No. 1.21.3.1

General information:

Sequence
show sequence in fasta format
  0 MGSVPVPVAN VPRIDVSPLF GDDKEKKLEV ARAIDAASRD TGFFYAVNHG VDLPWLSRET
 60 NKFHMSITDE EKWQLAIRAY NKEHESQIRA GYYLPIPGKK AVESFCYLNP SFSPDHPRIK
120 EPTPMHEVNV WPDEAKHPGF RAFAEKYYWD VFGLSSAVLR GYALALGRDE DFFTRHSRRD
180 TTLSSVVLIR YPYLDPYPEP AIKTADDGTK LSFEWHEDVS LITVLYQSDV QNLQVKTPQG
240 WQDIQADDTG FLINCGSYMA HITDDYYPAP IHRVKWVNEE RQSLPFFVNL GWEDTIQPWD
300 PATAKDGAKD AAKDKPAISY GEYLQGGLRG LINKNGQT
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
686493
Samson S.N.,Belagaje R.,Blankenship D.T.,Chapman J.L.,Perry D.,Skatrud P.L.,Vanfrank R.M.,Abraham E.P.,Baldwin J.E.,Queener S.W.,Ingolia T.D.
Isolation, sequence determination and expression in Escherichia coli of the isopenicillin N synthetase gene from Cephalosporium acremonium.
Nature
318
191-194
1985
686494
Ramsden M.,McQuade B.A.,Saunders K.,Turner M.K.,Harford S.
Characterization of a loss-of-function mutation in the isopenicillin N synthetase gene of Acremonium chrysogenum.
Gene
85
267-273
1989
686495
Baldwin J.E.,Gagnon J.,Ting H.H.
N-terminal amino acid sequence and some properties of isopenicillin-N synthetase from Cephalosporium acremonium.
FEBS Lett.
188
253-256
1985
686496
Baldwin J.E.,Coates J.B.,Moloney M.G.,Pratt A.J.,Willis A.C.
Photoaffinity labelling of isopenicillin N synthetase.
Biochem. J.
266
561-567
1990
686497
Tiow-Suan S.,Tan D.S.
Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity.
FEMS Microbiol. Lett.
120
241-247
1994
686498
Tan D.S.,Sim T.S.
Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.
J. Biol. Chem.
271
889-894
1996
686499
Loke P.,Sim J.,Sim T.S.
Functional analysis of a conserved aspartate D218 in Cephalosporium acremonium isopenicillin N synthase.
FEMS Microbiol. Lett.
157
137-140
1997
686500
Loke P.,Sim T.S.
Catalytic activity in Cephalosporium acremonium isopenicillin N synthase does not involve glutamine-234.
Biochem. Biophys. Res. Commun.
248
559-561
1998
686501
Loke P.,Sim T.S.
Analysis of glutamines in catalysis in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis.
Biochem. Biophys. Res. Commun.
252
472-475
1998
686502
Tan D.S.,Ang S.G.,Sim T.S.
Involvement of a third histidine in the ferrous active site of isopenicillin N synthase of Cephalosporium acremonium repudiated by recombinant double histidine mutants.
Biochem. Mol. Biol. Int.
44
333-345
1998
686503
Loke P.,Sim T.S.
Mutational evidence for the role of serine-283 in Cephalosporium acremonium isopenicillin N synthase.
FEMS Microbiol. Lett.
165
353-356
1998